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The TAFs of TFIID Bind and Rearrange the Topology of the TATA-Less RPS5 Promoter.


ABSTRACT: The general transcription factor TFIID is a core promoter selectivity factor that recognizes DNA sequence elements and nucleates the assembly of a pre-initiation complex (PIC). The mechanism by which TFIID recognizes the promoter is poorly understood. The TATA-box binding protein (TBP) is a subunit of the multi-protein TFIID complex believed to be key in this process. We reconstituted transcription from highly purified components on a ribosomal protein gene (RPS5) and discovered that TFIID?TBP binds and rearranges the promoter DNA topology independent of TBP. TFIID?TBP binds ~200 bp of the promoter and changes the DNA topology to a larger extent than the nucleosome core particle. We show that TBP inhibits the DNA binding activities of TFIID?TBP and conclude that the complete TFIID complex may represent an auto-inhibited state. Furthermore, we show that the DNA binding activities of TFIID?TBP are required for assembly of a PIC poised to select the correct transcription start site (TSS).

SUBMITTER: Le SN 

PROVIDER: S-EPMC6650902 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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The TAFs of TFIID Bind and Rearrange the Topology of the TATA-Less <i>RPS5</i> Promoter.

Le Sarah N SN   Brown Christopher R CR   Harvey Stacy S   Boeger Hinrich H   Elmlund Hans H   Elmlund Dominika D  

International journal of molecular sciences 20190704 13


The general transcription factor TFIID is a core promoter selectivity factor that recognizes DNA sequence elements and nucleates the assembly of a pre-initiation complex (PIC). The mechanism by which TFIID recognizes the promoter is poorly understood. The TATA-box binding protein (TBP) is a subunit of the multi-protein TFIID complex believed to be key in this process. We reconstituted transcription from highly purified components on a ribosomal protein gene (<i>RPS5</i>) and discovered that TFII  ...[more]

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